Characterisation of autolytic enzymes in Lactobacillus pentosus

Chartier, Marie Pierre Chapot

Yayın:
Characterisation of autolytic enzymes in Lactobacillus pentosus

dc.contributor.author	Chartier, Marie Pierre Chapot
dc.contributor.buuauthor	Çibik, Recep
dc.contributor.department	Veteriner Fakültesi
dc.contributor.department	Besin Hijyeni ve Teknolojisi Ana Bilim Dalı
dc.contributor.scopusid	56010542400
dc.date.accessioned	2022-04-21T06:23:36Z
dc.date.available	2022-04-21T06:23:36Z
dc.date.issued	2004
dc.description.abstract	Aims: To characterize autolysis and autolytic system of the lactic acid bacterium Lactobacillus pentosus. Methods and Results: Autolysis of nine Lact. pentosus strains was evaluated in buffer solution. Their peptidoglycan hydrolase profiles were examined by renaturing SDS-PAGE and revealed two major activity bands at 58 and 112 kDa. Specificity analysis indicated the presence of at least two different types of peptidoglycan hydrolase activities in Lact. pentosus 1091. Conclusions: Autolysis of Lact. pentosus was shown to be strain dependent and involvement of at least two different autolysins was evidenced. Significance and Impact of the Study: The autolytic system of Lact. pentosus was characterized for the first time and the data obtained could be used in the selection of strains of technological interest.
dc.identifier.citation	Çibik, R. ve Chartier, M. P. C. (2004). “Characterisation of autolytic enzymes in Lactobacillus pentosus”. Letters in Applied Microbiology, 38(6), 459-463.
dc.identifier.doi	10.1111/j.1472-765X.2004.01516.x
dc.identifier.endpage	463
dc.identifier.issn	0266-8254
dc.identifier.issue	6
dc.identifier.pubmed	15130139
dc.identifier.scopus	2-s2.0-2642540907
dc.identifier.startpage	459
dc.identifier.uri	https://doi.org/10.1111/j.1472-765X.2004.01516.x
dc.identifier.uri	https://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/j.1472-765X.2004.01516.x
dc.identifier.uri	http://hdl.handle.net/11452/25922
dc.identifier.volume	38
dc.identifier.wos	000221256600003
dc.indexed.wos	SCIE
dc.language.iso	en
dc.publisher	Wiley
dc.relation.collaboration	Yurt dışı
dc.relation.journal	Letters in Applied Microbiology
dc.relation.publicationcategory	Makale - Uluslararası Hakemli Dergi
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	Biotechnology and applied microbiology
dc.subject	Microbiology
dc.subject	Bacteria (microorganisms)
dc.subject	Lactobacillus
dc.subject	Lactobacillus pentosus
dc.subject	Posibacteria
dc.subject	Autolysis
dc.subject	Nonstarter lactic acid bacteria
dc.subject	Peptidoglycan hydrolase
dc.subject	Renaturing SDS-PAGE
dc.subject	Lactic-acid bacteria
dc.subject	Lactococcus-lactis
dc.subject	Cheese
dc.subject	Strains
dc.subject	Identification
dc.subject	Proteolysis
dc.subject	Phenotype
dc.subject	Prophage
dc.subject	Cheddar
dc.subject.emtree	Article
dc.subject.emtree	Autolysis
dc.subject.emtree	Bacterial strain
dc.subject.emtree	Controlled study
dc.subject.emtree	Enzyme activity
dc.subject.emtree	Lactobacillus
dc.subject.emtree	Lactobacillus pentosus
dc.subject.emtree	Nonhuman
dc.subject.emtree	Polyacrylamide gel electrophoresis
dc.subject.emtree	Autolysin
dc.subject.emtree	Buffer
dc.subject.emtree	Enzyme
dc.subject.emtree	Hydrolase
dc.subject.emtree	Lactic acid
dc.subject.emtree	Peptidoglycan
dc.subject.mesh	Bacteriolysis
dc.subject.mesh	Carbohydrates
dc.subject.mesh	Densitometry
dc.subject.mesh	Electrophoresis, polyacrylamide gel
dc.subject.mesh	Food microbiology
dc.subject.mesh	Lactobacillus
dc.subject.mesh	Molecular weight
dc.subject.mesh	N-acetylmuramoyl-l-alanine amidase
dc.subject.mesh	Substrate specificity
dc.subject.scopus	Cheese Ripening; Cheese; Rennet
dc.subject.wos	Biotechnology and applied microbiology
dc.subject.wos	Microbiology
dc.title	Characterisation of autolytic enzymes in Lactobacillus pentosus
dc.type	Article
dspace.entity.type	Publication
local.contributor.department	Veteriner Fakültesi/Besin Hijyeni ve Teknolojisi Ana Bilim Dalı
local.indexed.at	PubMed
local.indexed.at	WOS